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Volumn 55, Issue 25, 2007, Pages 10156-10161

Isolation and biochemical characterization of an antifungal peptide from Amaranthus hypochondriacus seeds

Author keywords

Amaranthus hypochondriacus; Antifungal activity; Antifungal peptide; Chitin binding peptide; Peptide purification

Indexed keywords

ALTERNARIA ALTERNATA; AMARANTHUS; AMARANTHUS HYPOCHONDRIACUS; ASPERGILLUS; ASPERGILLUS CANDIDUS; CANDIDA ALBICANS; FUNGI; FUSARIUM SOLANI; GALACTOMYCES GEOTRICHUM; PENICILLIUM CHRYSOGENUM; TRICHODERMA;

EID: 38049008017     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf072069x     Document Type: Article
Times cited : (36)

References (39)
  • 2
    • 0008135224 scopus 로고
    • Three-dimensional structure of phoratoxin in solution: Combined use of nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Clore, G. M.; Sukumaran, D. K.; Nilges, M.; Gronenborn, A. M. Three-dimensional structure of phoratoxin in solution: Combined use of nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry 1987, 26, 1732-1745.
    • (1987) Biochemistry , vol.26 , pp. 1732-1745
    • Clore, G.M.1    Sukumaran, D.K.2    Nilges, M.3    Gronenborn, A.M.4
  • 3
    • 0037409570 scopus 로고    scopus 로고
    • Common structural properties specifically found in the CS αβ-type antimicrobial peptides in nematodes and mollusks: Evidence for the same evolutionary origin
    • Zhang Hong Kato, Y. Common structural properties specifically found in the CS αβ-type antimicrobial peptides in nematodes and mollusks: Evidence for the same evolutionary origin. Dev. Comp. Immunol. 2003, 27, 499-503.
    • (2003) Dev. Comp. Immunol , vol.27 , pp. 499-503
    • Zhang Hong Kato, Y.1
  • 4
    • 0029379573 scopus 로고    scopus 로고
    • Cammue, B. P. A.; Thevissen, K.; Hendriks, M.; Eggermont, K; Goderis, I. J.; Proost, P.; Van Damme, J.; Osborn, R. W.; Guerbette, F.; Kader, J. C.; Broekaert, W. F. A potent antimicrobial protein from onion seeds showing sequence homology to plant lipid transfer proteins. Plant Physiol. 1995, 109, 445-455.
    • Cammue, B. P. A.; Thevissen, K.; Hendriks, M.; Eggermont, K; Goderis, I. J.; Proost, P.; Van Damme, J.; Osborn, R. W.; Guerbette, F.; Kader, J. C.; Broekaert, W. F. A potent antimicrobial protein from onion seeds showing sequence homology to plant lipid transfer proteins. Plant Physiol. 1995, 109, 445-455.
  • 7
    • 1542373564 scopus 로고    scopus 로고
    • Antifungal proteins: Targets, mechanisms and prospective applications
    • Theis, T.; Stahl, U. Antifungal proteins: Targets, mechanisms and prospective applications. Cell. Mol. Life Sci. 2004, 61, 437-455.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 437-455
    • Theis, T.1    Stahl, U.2
  • 8
    • 11944249594 scopus 로고
    • Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis)
    • Broekaert, W.; Lee, H. I.; Kush, A.; Chua, N. H.; Raikhel, N. Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis). Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 7633-7637.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 7633-7637
    • Broekaert, W.1    Lee, H.I.2    Kush, A.3    Chua, N.H.4    Raikhel, N.5
  • 9
    • 0002886806 scopus 로고
    • Chitinase in bean leaves: Induction by ethylene, purification, properties and possible function
    • Boiler, T.; Gehri, A.; Mauch, F.; Vogeli, U. Chitinase in bean leaves: Induction by ethylene, purification, properties and possible function. Planta 1983, 157, 22-31.
    • (1983) Planta , vol.157 , pp. 22-31
    • Boiler, T.1    Gehri, A.2    Mauch, F.3    Vogeli, U.4
  • 11
    • 0023130821 scopus 로고
    • Regulation of a plant pathogenesis-related enzyme: Inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin
    • Shinshi, H.; Mohnene, D.; Meins, F. Regulation of a plant pathogenesis-related enzyme: Inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin. Proc. Natl. Acad. Sci. U.S.A. 1987, 84, 89-93.
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 89-93
    • Shinshi, H.1    Mohnene, D.2    Meins, F.3
  • 12
  • 13
    • 0020119169 scopus 로고
    • Isolation and partial characterization of wheat-germ-agglutinin-like lectins from rye (Secale cereale) and barley (Hordeum vulgare) embryos
    • Peumans, W. J.; Stinissen, H. M.; Carlier, A. R. Isolation and partial characterization of wheat-germ-agglutinin-like lectins from rye (Secale cereale) and barley (Hordeum vulgare) embryos. Biochem. J. 1982, 203, 239-243.
    • (1982) Biochem. J , vol.203 , pp. 239-243
    • Peumans, W.J.1    Stinissen, H.M.2    Carlier, A.R.3
  • 14
    • 0018537777 scopus 로고
    • Purification and characterization of a lectin from rice bran
    • Tsuda, M. Purification and characterization of a lectin from rice bran. J. Biochem. 1979, 86, 1451-1461.
    • (1979) J. Biochem , vol.86 , pp. 1451-1461
    • Tsuda, M.1
  • 19
    • 0031048304 scopus 로고    scopus 로고
    • Characterization of a new antifungal chitin-binding peptide from sugar beet leaves
    • Nielsen, K. K.; Nielsen, J. E.; Madrid, S. M.; Mikkelsen, J. D. Characterization of a new antifungal chitin-binding peptide from sugar beet leaves. Plant Physiol. 1997, 113, 83-91.
    • (1997) Plant Physiol , vol.113 , pp. 83-91
    • Nielsen, K.K.1    Nielsen, J.E.2    Madrid, S.M.3    Mikkelsen, J.D.4
  • 21
    • 0037134784 scopus 로고    scopus 로고
    • Two novel antifungal peptides distinct with a 5-disulfide motif from the bark of Eucommia ulmoides Oliv
    • Huang, R. H.; Xiang, Y.; Liu, X. Z.; Zhang, Y.; Hu, Z.; Wang, D. C. Two novel antifungal peptides distinct with a 5-disulfide motif from the bark of Eucommia ulmoides Oliv. FEBS Lett. 2002, 521, 87-90.
    • (2002) FEBS Lett , vol.521 , pp. 87-90
    • Huang, R.H.1    Xiang, Y.2    Liu, X.Z.3    Zhang, Y.4    Hu, Z.5    Wang, D.C.6
  • 22
    • 0034726049 scopus 로고    scopus 로고
    • Characteristics and antifungal activity of a chitin-binding protein from Ginkgo biloba
    • Huang, X.; Xie, W.; Gong, Z. Characteristics and antifungal activity of a chitin-binding protein from Ginkgo biloba. FEBS Lett. 2000, 478, 123-126.
    • (2000) FEBS Lett , vol.478 , pp. 123-126
    • Huang, X.1    Xie, W.2    Gong, Z.3
  • 23
    • 0037834897 scopus 로고    scopus 로고
    • Amino acid sequence, biochemical characterization and comparative modeling of nonspecific lipid transfer protein from Amaranthus hypochondriacus
    • Ramírez, M.; Aguilar, M.; Miguel, R.; Bolaños, V.; García, E.; Soriano-Garcìa, M. Amino acid sequence, biochemical characterization and comparative modeling of nonspecific lipid transfer protein from Amaranthus hypochondriacus. Arch. Biochem. Biophys. 2003, 415, 24-33.
    • (2003) Arch. Biochem. Biophys , vol.415 , pp. 24-33
    • Ramírez, M.1    Aguilar, M.2    Miguel, R.3    Bolaños, V.4    García, E.5    Soriano-Garcìa, M.6
  • 24
    • 0037479662 scopus 로고    scopus 로고
    • Purification, crystallization, and preliminary X-ray characterization of a 36 kDa amaranth globulin
    • Vasco, N.; Soriano, M.; Moreno, A.; Castellanos, R.; Paredes, O. Purification, crystallization, and preliminary X-ray characterization of a 36 kDa amaranth globulin. J. Agric. Food Chem. 1999, 47, 862-866.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 862-866
    • Vasco, N.1    Soriano, M.2    Moreno, A.3    Castellanos, R.4    Paredes, O.5
  • 25
    • 11944249594 scopus 로고
    • Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis)
    • Broekaert, I.; Lee, H. I.; Kush, A.; Chua, N. H.; Raikhel, N. Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis). Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 7633-7637.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 7633-7637
    • Broekaert, I.1    Lee, H.I.2    Kush, A.3    Chua, N.H.4    Raikhel, N.5
  • 28
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from Polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm, M.; Shevchenko, A.; Houthaeve, T.; Breit, S.; Schweigerer, L.; Fotsis, T.; Mann, M. Femtomole sequencing of proteins from Polyacrylamide gels by nano-electrospray mass spectrometry. Nature 1996, 379, 466-169.
    • (1996) Nature , vol.379 , pp. 466-169
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 29
    • 34248586736 scopus 로고    scopus 로고
    • Identification of chitin binding proteins and characterization of two chitinases isoforms from Vibrio alginolyticus 283
    • Suginta, W. Identification of chitin binding proteins and characterization of two chitinases isoforms from Vibrio alginolyticus 283. Enzyme Microb. Technol. 2007, 41, 212-220.
    • (2007) Enzyme Microb. Technol , vol.41 , pp. 212-220
    • Suginta, W.1
  • 31
    • 0030730364 scopus 로고    scopus 로고
    • Genetic diversity and relationships detected by isozyme and RAPD analysis of crop and wild species of Amaranthus
    • Chan, K. F.; Sun, M. Genetic diversity and relationships detected by isozyme and RAPD analysis of crop and wild species of Amaranthus. Theor. Appl. Genet. 1997, 95, 865-873.
    • (1997) Theor. Appl. Genet , vol.95 , pp. 865-873
    • Chan, K.F.1    Sun, M.2
  • 32
    • 38049050982 scopus 로고    scopus 로고
    • http://expasy/tools.
  • 33
    • 23944488734 scopus 로고    scopus 로고
    • Pelegrini, P. B.; Franco, O. L. Plant γ-thionins: Novel insights on the mechanism of action of a multi-functional class of defense proteins. Int. J. Biochem. Cell Biol. 2005, 37, 2239-2253.
    • Pelegrini, P. B.; Franco, O. L. Plant γ-thionins: Novel insights on the mechanism of action of a multi-functional class of defense proteins. Int. J. Biochem. Cell Biol. 2005, 37, 2239-2253.
  • 34
    • 1042278916 scopus 로고    scopus 로고
    • Interaction of antifungal plant defensins with fungal membrane components
    • Thevissen, K.; Ferket, K. K. A.; Fraçois, I. E. J. A.; Cammue, B. P. A. Interaction of antifungal plant defensins with fungal membrane components. Peptides 2003, 24, 1705-1712.
    • (2003) Peptides , vol.24 , pp. 1705-1712
    • Thevissen, K.1    Ferket, K.K.A.2    Fraçois, I.E.J.A.3    Cammue, B.P.A.4
  • 36
    • 0025959114 scopus 로고
    • Defensins: Endogenous antibiotic peptides of animal cells
    • Lehrer, R. I.; Ganz, T.; Selsted, M. E. Defensins: Endogenous antibiotic peptides of animal cells. Cell 1991, 64, 229-230.
    • (1991) Cell , vol.64 , pp. 229-230
    • Lehrer, R.I.1    Ganz, T.2    Selsted, M.E.3
  • 38
    • 0037134784 scopus 로고    scopus 로고
    • Two novel antifungal peptides distinct with a five-disulfide motif from the bark of Eucommia ulmoides Oliv
    • Huang, R.; Xiang, Y.; Lium, X.; Zhang, Y.; Hu, Z.; Wang, D. Two novel antifungal peptides distinct with a five-disulfide motif from the bark of Eucommia ulmoides Oliv. FEBS Lett. 2002, 521, 87-90.
    • (2002) FEBS Lett , vol.521 , pp. 87-90
    • Huang, R.1    Xiang, Y.2    Lium, X.3    Zhang, Y.4    Hu, Z.5    Wang, D.6
  • 39
    • 0001194009 scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • Roberts, W. K.; Selitrennikoff, C. P. Plant and bacterial chitinases differ in antifungal activity. J. Gen. Microbiol. 1989, 134, 169-176.
    • (1989) J. Gen. Microbiol , vol.134 , pp. 169-176
    • Roberts, W.K.1    Selitrennikoff, C.P.2


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